COBQ_RALSO
ID COBQ_RALSO Reviewed; 481 AA.
AC Q8XWT0;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 2.
DT 25-MAY-2022, entry version 100.
DE RecName: Full=Cobyric acid synthase {ECO:0000255|HAMAP-Rule:MF_00028};
GN Name=cobQ {ECO:0000255|HAMAP-Rule:MF_00028}; OrderedLocusNames=RSc2390;
GN ORFNames=RS02759;
OS Ralstonia solanacearum (strain GMI1000) (Pseudomonas solanacearum).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Ralstonia.
OX NCBI_TaxID=267608;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GMI1000;
RX PubMed=11823852; DOI=10.1038/415497a;
RA Salanoubat M., Genin S., Artiguenave F., Gouzy J., Mangenot S., Arlat M.,
RA Billault A., Brottier P., Camus J.-C., Cattolico L., Chandler M.,
RA Choisne N., Claudel-Renard C., Cunnac S., Demange N., Gaspin C., Lavie M.,
RA Moisan A., Robert C., Saurin W., Schiex T., Siguier P., Thebault P.,
RA Whalen M., Wincker P., Levy M., Weissenbach J., Boucher C.A.;
RT "Genome sequence of the plant pathogen Ralstonia solanacearum.";
RL Nature 415:497-502(2002).
CC -!- FUNCTION: Catalyzes amidations at positions B, D, E, and G on
CC adenosylcobyrinic A,C-diamide. NH(2) groups are provided by glutamine,
CC and one molecule of ATP is hydrogenolyzed for each amidation.
CC {ECO:0000255|HAMAP-Rule:MF_00028}.
CC -!- PATHWAY: Cofactor biosynthesis; adenosylcobalamin biosynthesis.
CC {ECO:0000255|HAMAP-Rule:MF_00028}.
CC -!- SIMILARITY: Belongs to the CobB/CobQ family. CobQ subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_00028}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAD16097.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AL646052; CAD16097.1; ALT_INIT; Genomic_DNA.
DR AlphaFoldDB; Q8XWT0; -.
DR SMR; Q8XWT0; -.
DR STRING; 267608.RSc2390; -.
DR PRIDE; Q8XWT0; -.
DR EnsemblBacteria; CAD16097; CAD16097; RSc2390.
DR KEGG; rso:RSc2390; -.
DR eggNOG; COG1492; Bacteria.
DR HOGENOM; CLU_019250_2_2_4; -.
DR OMA; EIHHGVA; -.
DR UniPathway; UPA00148; -.
DR Proteomes; UP000001436; Chromosome.
DR GO; GO:0015420; F:ABC-type vitamin B12 transporter activity; IEA:UniProtKB-UniRule.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR GO; GO:0009236; P:cobalamin biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
DR CDD; cd01750; GATase1_CobQ; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR Gene3D; 3.40.50.880; -; 1.
DR HAMAP; MF_00028; CobQ; 1.
DR InterPro; IPR029062; Class_I_gatase-like.
DR InterPro; IPR002586; CobQ/CobB/MinD/ParA_Nub-bd_dom.
DR InterPro; IPR033949; CobQ_GATase1.
DR InterPro; IPR004459; CobQ_synth.
DR InterPro; IPR011698; GATase_3.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR21343:SF1; PTHR21343:SF1; 1.
DR Pfam; PF01656; CbiA; 1.
DR Pfam; PF07685; GATase_3; 1.
DR SUPFAM; SSF52317; SSF52317; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00313; cobQ; 1.
DR PROSITE; PS51274; GATASE_COBBQ; 1.
PE 3: Inferred from homology;
KW Cobalamin biosynthesis; Glutamine amidotransferase; Reference proteome.
FT CHAIN 1..481
FT /note="Cobyric acid synthase"
FT /id="PRO_0000141324"
FT DOMAIN 244..431
FT /note="GATase cobBQ-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
FT ACT_SITE 325
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
FT ACT_SITE 423
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
SQ SEQUENCE 481 AA; 50686 MW; 35EAE418ED7486A3 CRC64;
MIQGTTSDAG KSTLVAGLCR IAHRAGVRVA PFKPQNMALN SAVTADGGEI GRAQALQAQA
AGLAPTVDMN PVLLKPNSDT GAQVIIHGRP RGDLNARAYH DYKPTAMAAV LASHGRLRAQ
YDLVLVEGAG SPAEVNLRAR DIANMGFAEA VDCPVVLVAD IDRGGVFAHL VGTLACLSES
ERARVTGFVI NRFRGDLSLL TPGLDWLTAQ TGKPVFGVLP YLQGLHLDAE DAVQTAQSAA
SGEVLRVVIP VLPRISNHTD FDALRAHPQV DVRMVGPGRP IPPADLVILP GSKSVQADLA
WLRAHGWDAA IARHLRYGGK LIGICGGMQM LGRRLRDPLG LEGRPGSLDG LGYLDFETTL
APAKQLRQVR GTLADGGAAL AGYEIHMGVT EGPALARPAV RLDDGRTDGA VSADGQILAT
YLHGLFDAPE ACRALLAWAG VREARAQDYA ALREASLERL ADTLRAHLDL PALFASLAVR
G